The chemistry of allergens XX. New antigens generated by pepsin hydrolysis of bovine milk proteins

Spies, Joseph R.; Stevan, Mary Ann; Stein, William J.; Coulson, E. J.

doi:10.1016/0021-8707(70)90132-2

Cited by 36 publications

(24 citation statements)

References 14 publications

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“…Animal experiments have shown that digestive products exhibit antigenic specificity difFerent from the parent proteins, as judged by sensitization of guinea pig uterus and production of precipitins (9); these are presumably based on IgG antibodies, not reagins. Antibodies to digestive products could conceivably develop in immunocompetent humans but this has not yet been shown to occur, or to be a basis of s^-mptomatic immune reactions after oral ingestion of food proteins.…”

Section: Components Of Hypersensitivity Reactions Tofoods the Intestimentioning

confidence: 99%

A Modern Clinical Approach to Food Hypersensitivity

May

Block

1978

Allergy

107

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Section: Components Of Hypersensitivity Reactions Tofoods the Intestimentioning

confidence: 99%

A Modern Clinical Approach to Food Hypersensitivity

May

Block

1978

Allergy

107

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“…The investigation for bovine whey-specific IgE by means of RAST, CRIE and skin test showed clearly that none of the patients with cow's milk intoler ance had a type I allergic reaction against antigens of cow's milk and cow hair and dandruff. However, it cannot be excluded that, as proposed by Spies et al [1972], specific IgE activity is directed against the proteolytic degradation products of milk which appear during digestion.…”

Section: Discussionmentioning

confidence: 99%

Occurrence of Specific Precipitins against Bovine Whey Proteins in Serum from Children with Gastrointestinal Disorders

Løwenstein¹,

Krasilnikoff²,

Bjerrum³

et al. 1977

Int Arch Allergy Immunol

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Children with cow’s milk intolerance, clinically non-confirmed cow’s milk intolerance, coeliac disease, non-confirmed malabsorption, other gastrointestinal disorders, and normal children were investigated for the presence of precipitins against 40 individual bovine whey proteins by means of the crossed immunoelectrophoresis with intermediate gel technique. In the various groups of children the amount and specificity of bovine whey precipitins were neither connected with the various gastrointestinal disorders nor with alternating diet and challenge with milk. Bovine whey-specific IgE could not be detected in any of the patients clinically suspected for cow’s milk intolerance by cutaneous test, RAST or CRIE. The immunoglobulin level of the patients investigated did not differ significantly from the normal ranges. It is concluded that investigations of serum precipitins against bovine whey proteins do not give any significant information concerning cow’s milk intolerance.

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“…The first dialysate (Dl) did not contain all of the new antigens common to D2-D6 which indicated the presence of at least two new antigens in D2-D6. There was also an indication of a third new antigen in D6 [16]. Six precipitating new antigens were demonstrated in the endofractions, 2 in E l, 2 in E2 and 2 in E3-E6.…”

mentioning

confidence: 89%

“…The term 'new antigen' is defined as an anti gen with a specificity distinct from that of the protein from which it was generated. It was previously demonstrated by Spies et al [15] that new antigens were generated by 8-min pepsin hydrolysis of /Mactoglobulin, «-lactalbumin and casein, and that two new antigens were so generated from bovine serum albumin. In a later study [16], /J-lactoglobulin was hydrolyzed with pepsin for six successive, 8-min periods during which approximately 90% of the original protein was split into fragments with a molecular weight of 12,000 or less.…”

mentioning

confidence: 99%

“…It was previously demonstrated by Spies et al [15] that new antigens were generated by 8-min pepsin hydrolysis of /Mactoglobulin, «-lactalbumin and casein, and that two new antigens were so generated from bovine serum albumin. In a later study [16], /J-lactoglobulin was hydrolyzed with pepsin for six successive, 8-min periods during which approximately 90% of the original protein was split into fragments with a molecular weight of 12,000 or less. Six dialysate fractions (D1-D6) and six endofractions (E1-E6) were separated from the hydrolysates and analyzed for the presence of new antigens by the Schultz-Dale and gel diffusion techniques, respectively.…”

mentioning

confidence: 99%

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Chemistry of Allergens

Spies¹,

Stevan²,

Stein³

et al. 1975

Int Arch Allergy Immunol

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Twelve new antigens previously have been demonstrated in the pepsin digests of milk proteins. The term ‘new antigen’ is defined as an antigen with a specificity distinct from that of the protein from which it was generated. Three new antigenic (α-, β-, and D2i) polypeptides and one nonantigenic γ-polypeptide have been isolated from the dialysates of six successive pepsin hydrolyses of β-lactoglobulin. The α- and β-ρolypeptídes were 1/5 and D2i was 1/10–1/20 as potent immunogens as precursor β-lactoglobulin as determined by the Schultz-Dale technique. The minimum observed amounts of new antigen eliciting maximum response of uterine strips in the Schultz-Dale tests were: α-D2, 50 ng; β-D2, 15 ng; β-D3, 10 ng; and D2i, 1,000 ng. Except for the α-polypeptide, the amino acid contents of the polypeptides differed markedly from that of β-lactoglobulin. The β-polypeptide has been tentatively identified as a 33 amino acid fragment of β-lactoglobulin (3,910 daltons). The γ-polypeptide has been tentatively identified as a 12 amino acid fragment of β-lactoglobulin (1,372 daltons).

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The chemistry of allergens XX. New antigens generated by pepsin hydrolysis of bovine milk proteins

Cited by 36 publications

References 14 publications

A Modern Clinical Approach to Food Hypersensitivity

A Modern Clinical Approach to Food Hypersensitivity

Occurrence of Specific Precipitins against Bovine Whey Proteins in Serum from Children with Gastrointestinal Disorders

Chemistry of Allergens

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